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Biased ligand bonds to make right calls—laboratory of signal transduction reveals molecular mechanism for functional selectivity of GPCR

Biased ligand bonds to make right calls—laboratory of signal transduction reveals molecular mechanism for functional selectivity of GPCR
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摘要 In a recent study, Professor Rui-Ping Xiao and her research group at Institute of Molecular Medicine of Peking Univer- sity has provided an essential experimental evidence to support the new paradigm of functional selectivity for G protein-coupled receptor (GPCR) signal transduction. The study was published online on May 15 in The Journal of Biological Chemistry [ 1 ]. In a recent study,Professor Rui-Ping Xiao and her research group at Institute of Molecular Medicine of Peking University has provided an essential experimental evidence to support the new paradigm of functional selectivity for G protein-coupled receptor(GPCR)signal transduction.The study was published online on May 15 in The Journal of Biological Chemistry[1].The GPCR superfamily,a class of membrane
作者 WANG Jue
出处 《Science China(Life Sciences)》 SCIE CAS 2014年第9期957-958,共2页 中国科学(生命科学英文版)
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  • 1Woo AY, Jozwiak K, Toll L, Tanga MJ, Kozocas JA, Jimenez L, Huang Y, Song Y, Plazinska A, Pajak K, Paul RK, Bernier M, Wainer IW, Xiao RP. Tyrosine 308 is necessary for ligand-directed Gs-biased signaling of β2-adrenoceptor. J Biol Chem, 2014, doi: 10.1074/jbc.M114.558882.
  • 2Xiao RP, Zhang SJ, Chakir K, Avdonin P, Zhu W, Bond RA, Balke CW, Lakatta EG, Cheng H. Enhanced G(i) signaling selectively negates b2-adrenergic receptor (AR)-but not b1-AR-mediated positive inotropic effect in myocytes from failing rat hearts. Circulation, 2003, 108: 1633-1639.

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